Secretory sphingomyelinase

被引:90
作者
Tabas, I
机构
[1] Columbia Univ, Dept Med, New York, NY 10032 USA
[2] Columbia Univ, Dept Anat & Cell Biol, New York, NY 10032 USA
关键词
sphingomyelinase; ceramide; lysosomes; atherogenesis; macrophages; endothelial cell;
D O I
10.1016/S0009-3084(99)00080-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Several physiologic and pathophysiologic processes in which sphingomyelinases (SMases) have been implicated may involve extracellular sphingomyelin (SM) hydrolysis. A candidate enzyme for these processes is a recently discovered SMase called secretory SMase, or S-SMase. S-SMase arises from the acid sphingomyelinase (ASM) gene via differential protein trafficking of a common protein precursor; this precursor can be targeted to either lysosomes or the Golgi secretory pathway. S-SMase is activated by physiologic levels of Zn2+, although the S-SMase from endothelial cells, which secrete abundant amounts of the enzyme, is partially Zn2+-independent. S-SMase functions best at acid pH but can hydrolyze certain physiologic substrates, such as atherogenic lipoproteins, at neutral pH. In endothelial cells, the secretion of S-SMase is regulated at the level of protein trafficking by inflammatory cytokines. Current work implicates a role for S-SMase in atherogenesis, and future work will be directed at understanding the potential roles of S-SMase in other processes, such as ceramide-mediated cell-signaling and the host inflammatory response. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:123 / 130
页数:8
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